Document Detail

Purification and characterization of β-xylosidase that is active for plant complex type N-glycans from tomato (Solanum lycopersicum): removal of core α1-3 mannosyl residue is prerequisite for hydrolysis of β1-2 xylosyl residue.
MedLine Citation:
PMID:  22933239     Owner:  NLM     Status:  Publisher    
In this study, we purified and characterized the β-xylosidase involved in the turnover of plant complex type N-glycans to homogeneity from mature red tomatoes. Purified β-xylosidase (β-Xyl'ase Le-1) gave a single band with molecular masses of 67 kDa on SDS-PAGE under a reducing condition and 60 kDa on gelfiltration, indicating that β-Xyl'ase Le-1 has a monomeric structure in plant cells. The N-terminal amino acid could not be identified owing to a chemical modification. When pyridylaminated (PA-) N-glycans were used as substrates, β-Xyl'ase Le-1 showed optimum activity at about pH 5 at 40 °C, suggesting that the enzyme functions in a rather acidic circumstance such as in the vacuole or cell wall. β-Xyl'ase Le-1 hydrolyzed the β1-2 xylosyl residue from Man(1)Xyl(1)GlcNAc(2)-PA, Man(1)Xyl(1)Fuc(1)GlcNAc(2)-PA, and Man(2)Xyl(1)Fuc(1)GlcNAc(2)-PA, but not that from Man(3)Xyl(1)GlcNAc(2)-PA or Man(3)Xyl(1)Fuc(1)GlcNAc(2)-PA, indicating that the α1-3 arm mannosyl residue exerts significant steric hindrance for the access of β-Xyl'ase Le-1 to the xylosyl residue, whereas the α1-3 fucosyl residue exerts little effect. These results suggest that the release of the β1-2 xylosyl residue by β-Xyl'ase Le-1 occurs at least after the removal the α-1,3-mannosyl residue in the core trimannosyl unit.
Daisuke Yokouchi; Natsuko Ono; Kosuke Nakamura; Megumi Maeda; Yoshinobu Kimura
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-8-30
Journal Detail:
Title:  Glycoconjugate journal     Volume:  -     ISSN:  1573-4986     ISO Abbreviation:  Glycoconj. J.     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-8-30     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8603310     Medline TA:  Glycoconj J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Department of Biofunctional Chemistry, Graduate School of Natural Science and Technology, Okayama University, Tsushima-Naka 1-1-1, Okayama, 700-8530, Japan.
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